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P21550

- ENOB_MOUSE

UniProt

P21550 - ENOB_MOUSE

Protein

Beta-enolase

Gene

Eno3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Appears to have a function in striated muscle development and regeneration.

    Catalytic activityi

    2-phospho-D-glycerate = phosphoenolpyruvate + H2O.

    Cofactori

    Magnesium. Required for catalysis and for stabilizing the dimer.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei158 – 1581SubstrateBy similarity
    Binding sitei167 – 1671SubstrateBy similarity
    Active sitei210 – 2101Proton donorBy similarity
    Metal bindingi245 – 2451MagnesiumBy similarity
    Metal bindingi293 – 2931MagnesiumBy similarity
    Binding sitei293 – 2931SubstrateBy similarity
    Metal bindingi318 – 3181MagnesiumBy similarity
    Binding sitei318 – 3181SubstrateBy similarity
    Active sitei343 – 3431Proton acceptorBy similarity
    Binding sitei394 – 3941SubstrateBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphopyruvate hydratase activity Source: MGI

    GO - Biological processi

    1. aging Source: Ensembl
    2. glycolytic process Source: UniProtKB-UniPathway
    3. response to drug Source: Ensembl
    4. skeletal muscle tissue regeneration Source: Ensembl

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi4.2.1.11. 3474.
    UniPathwayiUPA00109; UER00187.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-enolase (EC:4.2.1.11)
    Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Enolase 3
    Muscle-specific enolase
    Short name:
    MSE
    Skeletal muscle enolase
    Gene namesi
    Name:Eno3
    Synonyms:Eno-3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:95395. Eno3.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Localized to the Z line. Some colocalization with CKM at M-band By similarity.By similarity

    GO - Cellular componenti

    1. membrane Source: Ensembl
    2. phosphopyruvate hydratase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 434433Beta-enolasePRO_0000134108Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP21550.
    PaxDbiP21550.
    PRIDEiP21550.

    2D gel databases

    SWISS-2DPAGEP21550.
    UCD-2DPAGEP21550.

    PTM databases

    PhosphoSiteiP21550.

    Expressioni

    Tissue specificityi

    The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. In striated muscle, the fiber-type order of ENO3 expression is IIB > IIX > IIA > I.1 Publication

    Developmental stagei

    During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells. In hindleg muscle, first expressed at E15 after which, levels increase sharply between E15 and E17. A steep prenatal rise in expression accompanies the formation of secondary myofibers and the development of innervation. High levels continue throughout newborn and adult stages. Beginning at postnatal day 5, a second sharp increase in expression correlates with the definitive specialization of the myofibers. Later in development, mainly expressed in fast-twitch fibers. In cardiac muscle, first expressed in the embryo in the cardiac tube.2 Publications

    Inductioni

    Levels decrease in degenerating myofibers, and increase with their regeneration.

    Gene expression databases

    ArrayExpressiP21550.
    BgeeiP21550.
    CleanExiMM_ENO3.
    GenevestigatoriP21550.

    Interactioni

    Subunit structurei

    Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and ALDO. Also binds PLG and troponin, in vitro. Interacts with PNKD By similarity.By similarity

    Protein-protein interaction databases

    BioGridi199453. 2 interactions.
    IntActiP21550. 4 interactions.
    MINTiMINT-1855839.

    Structurei

    3D structure databases

    ProteinModelPortaliP21550.
    SMRiP21550. Positions 1-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni370 – 3734Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the enolase family.Curated

    Phylogenomic databases

    eggNOGiCOG0148.
    GeneTreeiENSGT00550000074560.
    HOGENOMiHOG000072174.
    HOVERGENiHBG000067.
    InParanoidiP21550.
    KOiK01689.
    OMAiGELYKNF.
    PhylomeDBiP21550.
    TreeFamiTF300391.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    HAMAPiMF_00318. Enolase.
    InterProiIPR000941. Enolase.
    IPR020810. Enolase_C.
    IPR029065. Enolase_C-like.
    IPR020809. Enolase_CS.
    IPR020811. Enolase_N.
    IPR029017. Enolase_N_like.
    [Graphical view]
    PANTHERiPTHR11902. PTHR11902. 1 hit.
    PfamiPF00113. Enolase_C. 1 hit.
    PF03952. Enolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001400. Enolase. 1 hit.
    PRINTSiPR00148. ENOLASE.
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    TIGRFAMsiTIGR01060. eno. 1 hit.
    PROSITEiPS00164. ENOLASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P21550-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR    50
    DGDKARYLGK GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT 100
    ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGN PDLVLPVPAF 150
    NVINGGSHAG NKLAMQEFMI LPVGASSFKE AMRIGAEVYH HLKGVIKAKY 200
    GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV VIGMDVAASE 250
    FYRNGKYDLD FKSPDDPARH ISGEKLGELY KNFIQNYPVV SIEDPFDQDD 300
    WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV 350
    TESIQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR 400
    SERLAKYNQL MRIEEALGDK AVFAGRKFRN PKAK 434
    Length:434
    Mass (Da):47,025
    Last modified:January 23, 2007 - v3
    Checksum:iA1F757D83709D2B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti234 – 2352AG → NA in AAA37554. (PubMed:2734297)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61600 Genomic DNA. Translation: CAA43797.1.
    X57747 mRNA. Translation: CAA40913.1.
    X62667 mRNA. Translation: CAA44540.1.
    AK002485 mRNA. Translation: BAB22137.1.
    BC013460 mRNA. Translation: AAH13460.1.
    M20745 mRNA. Translation: AAA37554.1.
    CCDSiCCDS24961.1.
    PIRiS17109. NOMSB.
    RefSeqiNP_001129534.1. NM_001136062.2.
    NP_001263214.1. NM_001276285.1.
    NP_031959.1. NM_007933.3.
    XP_006532225.1. XM_006532162.1.
    XP_006537193.1. XM_006537130.1.
    UniGeneiMm.251322.
    Mm.491763.

    Genome annotation databases

    EnsembliENSMUST00000072841; ENSMUSP00000072620; ENSMUSG00000060600.
    ENSMUST00000108548; ENSMUSP00000104188; ENSMUSG00000060600.
    ENSMUST00000170716; ENSMUSP00000128714; ENSMUSG00000060600.
    GeneIDi13808.
    KEGGimmu:13808.
    UCSCiuc007jvx.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61600 Genomic DNA. Translation: CAA43797.1 .
    X57747 mRNA. Translation: CAA40913.1 .
    X62667 mRNA. Translation: CAA44540.1 .
    AK002485 mRNA. Translation: BAB22137.1 .
    BC013460 mRNA. Translation: AAH13460.1 .
    M20745 mRNA. Translation: AAA37554.1 .
    CCDSi CCDS24961.1.
    PIRi S17109. NOMSB.
    RefSeqi NP_001129534.1. NM_001136062.2.
    NP_001263214.1. NM_001276285.1.
    NP_031959.1. NM_007933.3.
    XP_006532225.1. XM_006532162.1.
    XP_006537193.1. XM_006537130.1.
    UniGenei Mm.251322.
    Mm.491763.

    3D structure databases

    ProteinModelPortali P21550.
    SMRi P21550. Positions 1-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199453. 2 interactions.
    IntActi P21550. 4 interactions.
    MINTi MINT-1855839.

    PTM databases

    PhosphoSitei P21550.

    2D gel databases

    SWISS-2DPAGE P21550.
    UCD-2DPAGE P21550.

    Proteomic databases

    MaxQBi P21550.
    PaxDbi P21550.
    PRIDEi P21550.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000072841 ; ENSMUSP00000072620 ; ENSMUSG00000060600 .
    ENSMUST00000108548 ; ENSMUSP00000104188 ; ENSMUSG00000060600 .
    ENSMUST00000170716 ; ENSMUSP00000128714 ; ENSMUSG00000060600 .
    GeneIDi 13808.
    KEGGi mmu:13808.
    UCSCi uc007jvx.2. mouse.

    Organism-specific databases

    CTDi 2027.
    MGIi MGI:95395. Eno3.

    Phylogenomic databases

    eggNOGi COG0148.
    GeneTreei ENSGT00550000074560.
    HOGENOMi HOG000072174.
    HOVERGENi HBG000067.
    InParanoidi P21550.
    KOi K01689.
    OMAi GELYKNF.
    PhylomeDBi P21550.
    TreeFami TF300391.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00187 .
    BRENDAi 4.2.1.11. 3474.

    Miscellaneous databases

    NextBioi 284592.
    PROi P21550.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21550.
    Bgeei P21550.
    CleanExi MM_ENO3.
    Genevestigatori P21550.

    Family and domain databases

    Gene3Di 3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    HAMAPi MF_00318. Enolase.
    InterProi IPR000941. Enolase.
    IPR020810. Enolase_C.
    IPR029065. Enolase_C-like.
    IPR020809. Enolase_CS.
    IPR020811. Enolase_N.
    IPR029017. Enolase_N_like.
    [Graphical view ]
    PANTHERi PTHR11902. PTHR11902. 1 hit.
    Pfami PF00113. Enolase_C. 1 hit.
    PF03952. Enolase_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001400. Enolase. 1 hit.
    PRINTSi PR00148. ENOLASE.
    SUPFAMi SSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    TIGRFAMsi TIGR01060. eno. 1 hit.
    PROSITEi PS00164. ENOLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Lamande N., Brosset S., Keller A., Lucas M., Lazar M.
      Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: BALB/c and Swiss Webster.
      Tissue: Liver and Skeletal muscle.
    2. "Beta-enolase is a marker of human myoblast heterogeneity prior to differentiation."
      Peterson C.A., Cho M., Rastinejad F., Blau H.M.
      Dev. Biol. 151:626-629(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C3H.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Kidney.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Colon.
    5. Lubec G., Kang S.U., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 33-50; 104-120; 257-262; 336-358 AND 373-394, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    6. "Murine muscle-specific enolase: cDNA cloning, sequence, and developmental expression."
      Lamande N., Mazo A.M., Lucas M., Montarras D., Pinset C., Gros F., Legault-Demare L., Lazar M.
      Proc. Natl. Acad. Sci. U.S.A. 86:4445-4449(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-434.
    7. "Activation of the gene encoding the glycolytic enzyme beta-enolase during early myogenesis precedes an increased expression during fetal muscle development."
      Keller A., Ott M.O., Lamande N., Lucas M., Gros F., Buckingham M., Lazar M.
      Mech. Dev. 38:41-54(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVATION DURING MYOGENESIS.
    8. "Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy."
      Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.
      Am. J. Physiol. 269:H1843-H1851(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    9. "Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins."
      Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F., Lazar M., Keller A.
      Biochem. J. 323:791-800(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PKM; PGM; CKM; ALDO AND TROPONIN, DEVELOPMENTAL STAGE.
    10. "Fibre-type distribution and subcellular localisation of alpha and beta enolase in mouse striated muscle."
      Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C., Lucas M., Chatelet F.-P.
      Biol. Cell 92:527-535(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "Differential modulation of alpha, beta and gamma enolase isoforms in regenerating mouse skeletal muscle."
      Merkulova T., Dehaupas M., Nevers M.C., Creminon C., Alameddine H., Keller A.
      Eur. J. Biochem. 267:3735-3743(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: EXPRESSION REGULATION.

    Entry informationi

    Entry nameiENOB_MOUSE
    AccessioniPrimary (citable) accession number: P21550
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3